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Titolo:
Dynamin family of mechanoenzymes
Autore:
Danino, D; Hinshaw, JE;
Indirizzi:
NIH, Lab Cell Biochem & Biol, Bethesda, MD 20892 USA NIH Bethesda MD USA 20892 Lab Cell Biochem & Biol, Bethesda, MD 20892 USA
Titolo Testata:
CURRENT OPINION IN CELL BIOLOGY
fascicolo: 4, volume: 13, anno: 2001,
pagine: 454 - 460
SICI:
0955-0674(200108)13:4<454:DFOM>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUANYLATE-BINDING PROTEIN-1; CLATHRIN-MEDIATED ENDOCYTOSIS; MITOCHONDRIAL-DNA MAINTENANCE; DOMINANT OPTIC ATROPHY; HUMAN MXB PROTEIN; ARABIDOPSIS-THALIANA; SUBCELLULAR-LOCALIZATION; NUCLEOTIDE-BINDING; TARGET STRUCTURES; NERVE-TERMINALS;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Danino, D NIH, Lab Cell Biochem & Biol, Bldg 8,Room 419,MSC 0851,8 Ctr Dr,Bethesda,MD 20892 USA NIH Bldg 8,Room 419,MSC 0851,8 Ctr Dr Bethesda MD USA 20892 USA
Citazione:
D. Danino e J.E. Hinshaw, "Dynamin family of mechanoenzymes", CURR OP CEL, 13(4), 2001, pp. 454-460

Abstract

The dynamin family of proteins is continually growing, and in recent yearsmembers have been localized to areas of mitochondrial fission, plant phragmoplasts and chloroplasts, and viral ribonucleoprotein complexes. All the dynamin-like proteins examined to-date appear to assemble into oligomers, such as rings or spirals; however, it remains to be determined if a global mechanism of action exists. Even the role of dynamin in vesicle formation remains controversial as to whether it behaves as a molecular switch or as a mechanochemical enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/10/20 alle ore 10:52:19